Covalent coupling of bovine growth hormone to its receptor in bovine liver membranes. Academic Article

abstract

• The structure of bovine somatotropin receptor was examined following covalent coupling of iodinated recombinant bovine growth hormone ([125I]rbGH) to bovine liver membrane receptors using ethylene glycol bis(succinimidyl succinate). Iodinated rbGH was incorporated into a complex of estimated Mr of 140,000 under reducing conditions. Excess unlabeled rbGH, but not bovine prolactin (bPRL), inhibited completely the incorporation of [125I]rbGH into the Mr = 140,000 species. In dairy bulls, the Mr = 140,000 complex was undetectable soon after birth but became predominant at 6 months of age. No evidence was found to support presence of bPRL receptors in steer liver membranes. Assuming a 1:1 stoichiometry of hormone binding to receptor, it appears that bGH binds to a major receptor subunit of Mr = 119,000 which does not recognize bPRL.

authors

• Bazer, Fuller

published proceedings

• Mol Cell Endocrinol

author list (cited authors)

• Badinga, L., Collier, R. J., Thatcher, W. W., Quintana, S. J., & Bazer, F. W.

citation count

• 11

complete list of authors

• Badinga, L||Collier, RJ||Thatcher, WW||Quintana, SJ||Bazer, FW

publication date

• July 1987

publisher

• Elsevier  Publisher

published in

• Molecular and Cellular Endocrinology  Journal

keywords

• Animals
• Cattle
• Cell Membrane
• Cross-Linking Reagents
• Growth Hormone
• Kinetics
• Liver
• Male
• Molecular Weight
• Receptors, Somatotropin
• Recombinant Proteins
• Succinimides

PubMed Central ID

• 3622922

Digital Object Identifier (DOI)

• 10.1016/0303-7207(87)90100-6

start page

• 85

end page

• 89

volume

• 52

issue

• 1-2

URL

• http://dx.doi.org/10.1016/0303-7207(87)90100-6